TRIM23 (Kr.5q12.3) ARFD1, ARD1, RNF46

(Tässä TRIM23:llsa on poikkeuksellinen domaani ARF. koska se osallistuu myös inositidien aineenvaihduntaan, asetin siitä teitoa PhytinFytiini-blogiini).

https://naturemicrobiologycommunity.nature.com/users/62261-michaela-gack/posts/19910-trim23-a-new-player-in-virus-induced-autophagy




 

TRIM23 Kr.5q12.3. ARFD1. ARD1. RNF46

PubMed Gene- Geenin TRIMN23 koodaama proteiini kuuluu TRIMperheeseen: Siinä on kolme sinkkiä sitovaa domeenia, RING-domeeni ja B-box 1 ja B-box2 sekä CC (coiled coil) alue. Tämä proteiini kuuluu guaniininukleotidejä (Gtp-Gdp) sitovaan ARF- perheeseen (ADP-ribosylaatiotekijäperheeseen). Sen C-terminaalissa on ARF-domeeni ja guaniininukleotidia sitova kohta, kun taas aminoterminaalissa ( N-terminaalissa) on GTPaasin aktivoiva proteiinidomeeni, mikä vaikuttaa guaniininukleotidia sitovaan kohtaan. Tämä TRIM-proteiini lokalisoituu lysosomiin ja Golgin laitteeseen. Sillä on merkitystä solunsisäisten kuljetusrakkuloiden muodostamisessa, niiden liikkumisessa aitosta toiseen ja PLD-aktivaatiossa. On kolme alternatiivista transkriptivarianttia tästä geenistä, alfa, beeta ja gamma. C-terminaaliessa on jokaisella jotain tyypillistä omaa rakennetta.  Sitä ilmenee yleisesti aivossa (eniten ), myös prostatasa ja 24 muussa kudoksessa.
https://www.ncbi.nlm.nih.gov/gene/373

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein is also a member of the ADP ribosylation factor family of guanine nucleotide-binding family of proteins. Its carboxy terminus contains an ADP-ribosylation factor domain and a guanine nucleotide binding site, while the amino terminus contains a GTPase activating protein domain which acts on the guanine nucleotide binding site. The protein localizes to lysosomes and the Golgi apparatus. It plays a role in the formation of intracellular transport vesicles, their movement from one compartment to another, and phopholipase D activation. Three alternatively spliced transcript variants for this gene have been described. [provided by RefSeq, Jul 2008] Expression Ubiquitous expression in brain (RPKM 18.0), prostate (RPKM 7.0) and 24 other tissues See more elated articles in PubMed

Related articles in PubMed

1. Identification of lysosomal and Golgi localization signals in GAP and ARF domains of ARF domain protein 1. Vitale N, et al. Mol Cell Biol, 2000 Oct. PMID 10982851, Free PMC Article
2. Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1). Vitale N, et al. J Biol Chem, 1998 Jan 30. PMID 9446556
3. Characterization of a GDP dissociation inhibitory region of ADP-ribosylation factor domain protein ARD1. Vitale N, et al. J Biol Chem, 1997 Oct 3. PMID 9312116
4. Localization of ADP-ribosylation factor domain protein 1 (ARD1) in lysosomes and Golgi apparatus. Vitale N, et al. Proc Natl Acad Sci U S A, 1998 Jul 21. PMID 9671726, Free PMC Article
5. ARD1, a 64-kDa bifunctional protein containing an 18-kDa GTP-binding ADP-ribosylation factor domain and a 46-kDa GTPase-activating domain. Vitale N, et al. Proc Natl Acad Sci U S A, 1996 Mar 5. PMID 8700863, Free PMC Article
   

See all (37) citations in PubMed

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

• Our results indicate that TRIM23 enzymatic activity requires RING dimerization, consistent with the general model of TRIM activation

• TRIM23 regulates adipocyte differentiation via stabilization of the adipogenic activator PPARgamma2.

• conclude that TRIM23-mediated ubiquitin conjugation to NEMO is essential for TLR3- and RIG-I/MDA5-mediated antiviral innate and inflammatory responses

• The authors present a novel role for TRIM23 that is specific to UL144-mediated activation of NF-kappaB during the course of virus infection.

• Data are consistent with a potential function for ADP-ribosylation factor domain protein 1 as an E3 ubiquitin ligase in cells.
   
  
• Isoformi alfa /product="E3 ubiquitin-protein ligase TRIM23 isoformhttps://www.ncbi.nlm.nih.gov/protein/NP_001647.1
  

           ORIGIN      
        1 matlvvnklg agvdsgrqgs rgtavvkvle cgvcedvfsl qgdkvprlll cghtvchdcl
       61 trlplhgrai rcpfdrqvtd lgdsgvwglk knfallelle rlqngpigqy gaaeesigis
      121 gesiircded eahlasvyct vcathlcsec sqvthstktl akhrrvplad kphektmcsq
      181 hqvhaiefvc leegcqtspl mccvckeygk hqghkhsvle peanqirasi ldmahcirtf
      241 teeisdysrk lvgivqhieg geqivedgig mahtehvpgt aenarscira yfydlhetlc
      301 rqeemalsvv dahvrekliw lrqqqedmti llsevsaacl hcektlqqdd crvvlakqei
      361 trlletlqkq qqqftevadh iqldasipvt ftkdnrvhig pkmeirvvtl gldgagktti
      421 lfklkqdefm qpiptigfnv etveyknlkf tiwdvggkhk lrplwkhyyl ntqavvfvvd
      481 sshrdrisea hselakllte kelrdallli fankqdvaga lsveeitell slhklccgrs
      541 wyiqgcdars gmglyegldw lsrqlvaagv ldva
/
http://www.med.u-fukui.ac.jp/SEIKA2/ED-Genes/TCDD/RL95-2TCDD/other/TRIM23.html

• isoformi beta
  

• ORIGIN      

        1 matlvvnklg agvdsgrqgs rgtavvkvle cgvcedvfsl qgdkvprlll cghtvchdcl
       61 trlplhgrai rcpfdrqvtd lgdsgvwglk knfallelle rlqngpigqy gaaeesigis
      121 gesiircded eahlasvyct vcathlcsec sqvthstktl akhrrvplad kphektmcsq
      181 hqvhaiefvc leegcqtspl mccvckeygk hqghkhsvle peanqirasi ldmahcirtf
      241 teeisdysrk lvgivqhieg geqivedgig mahtehvpgt aenarscira yfydlhetlc
      301 rqeemalsvv dahvrekliw lrqqqedmti llsevsaacl hcektlqqdd crvvlakqei
      361 trlletlqkq qqqftevadh iqldasipvt ftkdnrvhig pkmeirvvtl gldgagktti
      421 lfklkqdefm qpiptigfnv etveyknlkf tiwdvggkhk lrplwkhyyl ntqavvfvvd
      481 sshrdrisea hselakllte kelrdallli fankqdvaga lsveeitell slhklccgrs
      541 wyiqgcdars vfqiicdqyt gkevvtekg
//

• https://www.ncbi.nlm.nih.gov/pubmed/25905670
  
• http://www.med.u-fukui.ac.jp/SEIKA2/ED-Genes/TCDD/RL95-2TCDD/other/TRIM23.html